Examining the Influence of Phosphorylation on Peptide Ion Structure by Ion Mobility Spectrometry-Mass Spectrometry |
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| Authors: | Matthew S. Glover Jonathan M. Dilger Matthew D. Acton Randy J. Arnold Predrag Radivojac David E. Clemmer |
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| Affiliation: | 1.Department of Chemistry,Indiana University,Bloomington,USA;2.Spectrum Warfare Systems Department,NSWC Crane Division,Crane,USA;3.AB SCIEX,Vaughan,Canada;4.Department of Computer Science and Informatics,Indiana University,Bloomington,USA |
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| Abstract: | Ion mobility spectrometry-mass spectrometry (IMS-MS) techniques are used to study the general effects of phosphorylation on peptide structure. Cross sections for a library of 66 singly phosphorylated peptide ions from 33 pairs of positional isomers, and unmodified analogues were measured. Intrinsic size parameters (ISPs) derived from these measurements yield calculated collision cross sections for 85% of these phosphopeptide sequences that are within ±2.5% of experimental values. The average ISP for the phosphoryl group (0.64 ± 0.05) suggests that in general this moiety forms intramolecular interactions with the neighboring residues and peptide backbone, resulting in relatively compact structures. We assess the capability of ion mobility to separate positional isomers (i.e., peptide sequences that differ only in the location of the modification) and find that more than half of the isomeric pairs have >1% difference in collision cross section. Phosphorylation is also found to influence populations of structures that differ in the cis/trans orientation of Xaa–Pro peptide bonds. Several sequences with phosphorylated Ser or Thr residues located N-terminally adjacent to Pro residues show fewer conformations compared to the unmodified sequences. |
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